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5DPE

Thermolysin in complex with inhibitor.

Functional Information from GO Data
ChainGOidnamespacecontents
E0004222molecular_functionmetalloendopeptidase activity
E0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues21
Detailsbinding site for residue 5H8 E 401
ChainResidue
ETYR106
ETYR157
EGLU166
ELEU202
EARG203
EHIS231
EZN402
EDMS409
EDMS409
EGOL411
EHOH572
EASN111
EHOH629
EHOH679
EASN112
EALA113
EPHE114
ETRP115
EHIS142
EGLU143
EHIS146

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN E 402
ChainResidue
EHIS142
EHIS146
EGLU166
E5H8401

site_idAC3
Number of Residues6
Detailsbinding site for residue CA E 403
ChainResidue
EASP138
EGLU177
EASP185
EGLU187
EGLU190
EHOH602

site_idAC4
Number of Residues6
Detailsbinding site for residue CA E 404
ChainResidue
EASP57
EASP59
EGLN61
EHOH556
EHOH605
EHOH780

site_idAC5
Number of Residues6
Detailsbinding site for residue CA E 405
ChainResidue
EGLU177
EASN183
EASP185
EGLU190
EHOH560
EHOH631

site_idAC6
Number of Residues6
Detailsbinding site for residue CA E 406
ChainResidue
ETYR193
ETHR194
EILE197
EASP200
EHOH615
EHOH751

site_idAC7
Number of Residues5
Detailsbinding site for residue DMS E 407
ChainResidue
EILE1
ETHR2
EGLY3
EGLN31
EASN33

site_idAC8
Number of Residues5
Detailsbinding site for residue DMS E 408
ChainResidue
EGLY95
EPRO184
ETRP186
EHOH666
EHOH688

site_idAC9
Number of Residues5
Detailsbinding site for residue DMS E 409
ChainResidue
ETYR110
EASN112
EPHE114
E5H8401
E5H8401

site_idAD1
Number of Residues6
Detailsbinding site for residue DMS E 410
ChainResidue
ETYR66
EHIS216
ESER218
ETYR251
EHOH867
EHOH873

site_idAD2
Number of Residues8
Detailsbinding site for residue GOL E 411
ChainResidue
EPHE114
ETRP115
EHIS146
ETYR157
E5H8401
EHOH513
EHOH536
EHOH703

site_idAD3
Number of Residues7
Detailsbinding site for residue GOL E 412
ChainResidue
EGLY109
ETYR110
EASN111
EASN112
EGLN158
EHOH616
EHOH756

site_idAD4
Number of Residues12
Detailsbinding site for residue GOL E 413
ChainResidue
EGLY247
EGLY248
ETHR249
EVAL255
EGLN273
ETYR274
ELEU275
EHOH553
EHOH558
EHOH654
EHOH667
EHOH766

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VVAHELTHAV
ChainResidueDetails
EVAL139-VAL148

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"4808703","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"4808703","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 176
ChainResidueDetails

239149

PDB entries from 2025-07-23

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